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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-1057

Osterwalder, T; Contartese, J; Stoeckli, E T; Kuhn, T B; Sonderegger, P (1996). Neuroserpin, an axonally secreted serine protease inhibitor. The EMBO Journal, 15(12):2944-2953.

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Abstract

We have identified and chromatographically purified an axonally secreted glycoprotein of CNS and PNS neurons. Several peptides derived from it were microsequenced. Based on these sequences, a fragment of the corresponding cDNA was amplified and used as a probe to isolate a full length cDNA from a chicken brain cDNA library. Because the deduced amino acid sequence qualified the protein as a novel member of the serpin family of serine protease inhibitors, we called it neuroserpin. Analysis of the primary structural features further characterized neuroserpin as a heparin-independent, functional inhibitor of a trypsin-like serine protease. In situ hybridization revealed a predominantly neuronal expression during the late stages of neurogenesis and in the adult brain in regions which exhibit synaptic plasticity. Thus, neuroserpin might function as an axonally secreted regulator of the local extracellular proteolysis involved in the reorganization of the synaptic connectivity during development and synapse plasticity in the adult.

Item Type:Journal Article, refereed
Communities & Collections:04 Faculty of Medicine > Institute of Biochemistry
07 Faculty of Science > Institute of Biochemistry
DDC:570 Life sciences; biology
Language:English
Date:17 June 1996
Deposited On:11 Feb 2008 13:20
Last Modified:27 Nov 2013 20:57
Publisher:European Molecular Biology Organization ; Nature Publishing Group
ISSN:0261-4189
Funders:Olga Mayenfisch-Stiftung, Union Bank of Switzerland on behalf of a client.
Related URLs:http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=8670795
PubMed ID:8670795
Citations:Web of Science®. Times Cited: 108
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